4dex: Difference between revisions

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 ==Crystal structure of the Voltage Dependent Calcium Channel beta-2 Subunit in Complex With The CaV2.2 I-II Linker.==
-<StructureSection load='4dex' size='340' side='right' caption='[[4dex]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
+<StructureSection load='4dex' size='340' side='right'caption='[[4dex]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4dex]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus] and [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4DEX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4DEX FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4dex]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus] and [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4DEX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4DEX FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1t3l|1t3l]], [[4dey|4dey]]</td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2&#8491;</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CACNB2, CACNLB2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9986 Oryctolagus cuniculus]), Cach5, Cacna1b, Cacnl1a5 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus])</td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4dex FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dex OCA], [https://pdbe.org/4dex PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4dex RCSB], [https://www.ebi.ac.uk/pdbsum/4dex PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4dex ProSAT]</span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4dex FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dex OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4dex RCSB], [http://www.ebi.ac.uk/pdbsum/4dex PDBsum]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/CACB2_RABIT CACB2_RABIT]] The beta subunit of voltage-dependent calcium channels contributes to the function of the calcium channel by increasing peak calcium current, shifting the voltage dependencies of activation and inactivation, modulating G protein inhibition and controlling the alpha-1 subunit membrane targeting.
+[https://www.uniprot.org/uniprot/CACB2_RABIT CACB2_RABIT] The beta subunit of voltage-dependent calcium channels contributes to the function of the calcium channel by increasing peak calcium current, shifting the voltage dependencies of activation and inactivation, modulating G protein inhibition and controlling the alpha-1 subunit membrane targeting.
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-Voltage-dependent calcium channels (VDCCs) allow the passage of Ca(2+) ions through cellular membranes in response to membrane depolarization. The channel pore-forming subunit, alpha1, and a regulatory subunit (Ca(V)beta) form a high affinity complex where Ca(V)beta binds to a alpha1 interacting domain in the intracellular linker between alpha1 membrane domains I and II (I-II linker). We determined crystal structures of Ca(V)beta2 functional core in complex with the Ca(V)1.2 and Ca(V)2.2 I-II linkers to a resolution of 1.95 and 2.0 A, respectively. Structural differences between the highly conserved linkers, important for coupling Ca(V)beta to the channel pore, guided mechanistic functional studies. Electrophysiological measurements point to the importance of differing linker structure in both Ca(V)1 and 2 subtypes with mutations affecting both voltage- and calcium-dependent inactivation and voltage dependence of activation. These linker effects persist in the absence of Ca(V)beta, pointing to the intrinsic role of the linker in VDCC function and suggesting that I-II linker structure can serve as a brake during inactivation.
-The role of a voltage-dependent Ca2+ channel intracellular linker: a structure-function analysis.,Almagor L, Chomsky-Hecht O, Ben-Mocha A, Hendin-Barak D, Dascal N, Hirsch JA J Neurosci. 2012 May 30;32(22):7602-13. PMID:22649239<ref>PMID:22649239</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+==See Also==
-</div>
+*[[Ion channels 3D structures|Ion channels 3D structures]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>
+[[Category: Large Structures]]
 [[Category: Oryctolagus cuniculus]]
 [[Category: Rattus norvegicus]]
-[[Category: Almagor, L]]
+[[Category: Almagor L]]
-[[Category: Hirsch, J A]]
+[[Category: Hirsch JA]]
-[[Category: Maguk]]
-[[Category: Transport protein]]
-[[Category: Voltage dependent calcium channel]]